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Gulnik SV, Eissenstat M. However, if the biological activity of such an enzyme needs to be maintained, one should consider using other types of serine protease inhibitor such as AEBSF, Aprotinin or Benzamidine.
Metalloproteases, on the other hand, are best deactivated by using EDTA that chelates the metal ions required for metalloproteases activity. Other classical lock and key inhibitors such as bestatin and other protein inhibitors such as alpha-2 macroglobulin can also be used.
Other proteases may be of lesser significance but they should likewise be rendered ineffective if you want to get accurate results from your assay. Protease inhibitors work by reversibly or irreversibly deactivating the protease present in the cell lysate by binding to the active site or by modifying its structure. Either of these actions will prevent the hydrolysis of the protein sample and allow you to store your lysate for a longer duration without being degraded in the process.
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